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PDBsum entry 2law

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protein Protein-protein interface(s) links
Signaling protein/transcription PDB id
2law

 

 

 

 

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Contents
Protein chains
34 a.a.
12 a.a.
PDB id:
2law
Name: Signaling protein/transcription
Title: Structure of the second ww domain from human yap in complex with a human smad1 derived peptide
Structure: Yorkie homolog. Chain: a. Fragment: second ww domain, residues 230-263. Synonym: 65 kda yes-associated protein, yap65. Engineered: yes. Mothers against decapentaplegic homolog 1. Chain: b. Fragment: residues 222-233. Synonym: mad homolog 1, mothers against dpp homolog 1, jv4-1, mad-
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: yap1, yap65. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
NMR struc: 20 models
Authors: M.J.Macias,E.Aragon,N.Goerner,A.Zaromytidou,Q.Xi,A.Escobedo, J.Massague
Key ref: E.Aragón et al. (2011). A Smad action turnover switch operated by WW domain readers of a phosphoserine code. Genes Dev, 25, 1275-1288. PubMed id: 21685363
Date:
22-Mar-11     Release date:   06-Jul-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P46937  (YAP1_HUMAN) -  Transcriptional coactivator YAP1 from Homo sapiens
Seq:
Struc:
504 a.a.
34 a.a.
Protein chain
Pfam   ArchSchema ?
Q15797  (SMAD1_HUMAN) -  Mothers against decapentaplegic homolog 1 from Homo sapiens
Seq:
Struc:
465 a.a.
12 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Genes Dev 25:1275-1288 (2011)
PubMed id: 21685363  
 
 
A Smad action turnover switch operated by WW domain readers of a phosphoserine code.
E.Aragón, N.Goerner, A.I.Zaromytidou, Q.Xi, A.Escobedo, J.Massagué, M.J.Macias.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22992590 J.Massagué (2012).
TGFβ signalling in context.
  Nat Rev Mol Cell Biol, 13, 616-630.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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